Research workbench
Mechanism of protease dependent dpc repair
Analyse Mechanism of protease dependent dpc repair in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MDW
- Type
- protein
- Length
- 185 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sprt-like domain-containing protein spartan
- UniProt
- Q9H040
- Ligands
- ADP, ZN
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sprt-like domain-containing protein spartan | protein | 185 | 32% helix, 16% strand | Q9H040 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- FLC · Citrate anion · additive · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 274 | 0.60 | 0.79 | 35 | FLC |
| 2 | 143 | 0.46 | 0.77 | 20 | ADP |
| 3 | 106 | 0.43 | 0.77 | 16 | empty |
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9H040
- Elsewhere: RCSB PDB 6MDW · PDBe 6MDW · UniProt Q9H040
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